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    Prima1 proline rich membrane anchor 1 [ Mus musculus (house mouse) ]

    Gene ID: 170952, updated on 13-Jan-2025

    Summary

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    Official Symbol
    Prima1provided by MGI
    Official Full Name
    proline rich membrane anchor 1provided by MGI
    Primary source
    MGI:MGI:1926097
    See related
    Ensembl:ENSMUSG00000041669 AllianceGenome:MGI:1926097
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Also known as
    PRiMA; B230212M13Rik
    Summary
    Enables enzyme binding activity and protein-membrane adaptor activity. Acts upstream of or within establishment of localization in cell. Located in plasma membrane. Orthologous to human PRIMA1 (proline rich membrane anchor 1). [provided by Alliance of Genome Resources, Jan 2025]
    Expression
    Broad expression in stomach adult (RPKM 7.2), bladder adult (RPKM 4.3) and 19 other tissues See more
    Orthologs
    human all
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    Genomic context

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    See Prima1 in Genome Data Viewer
    Location:
    12 E; 12 52.9 cM
    Exon count:
    7
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 12 NC_000078.7 (103160712..103208967, complement)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 12 NC_000078.6 (103194453..103242719, complement)

    Chromosome 12 - NC_000078.7Genomic Context describing neighboring genes Neighboring gene cytochrome c oxidase subunit 8C Neighboring gene unc-79 homolog Neighboring gene STARR-seq mESC enhancer starr_33121 Neighboring gene STARR-positive B cell enhancer ABC_E7173 Neighboring gene CapStarr-seq enhancer MGSCv37_chr12:104569739-104569961 Neighboring gene STARR-positive B cell enhancer ABC_E4038 Neighboring gene family with sequence similarity 181, member A Neighboring gene STARR-positive B cell enhancer ABC_E1863 Neighboring gene predicted gene 29508 Neighboring gene predicted gene 15523 Neighboring gene ankyrin repeat and SOCS box-containing 2

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Mouse ENCODE transcriptome data
    • Description: RNA profiling data sets generated by the Mouse ENCODE project.
    • BioProject: PRJNA66167
    • Publication: PMID 25409824
    • Analysis date: n/a

    Bibliography

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    Related articles in PubMed

    1. Schwann cells sense and control acetylcholine spillover at the neuromuscular junction by α7 nicotinic receptors and butyrylcholinesterase. Petrov KA, et al. J Neurosci, 2014 Sep 3. PMID 25186736, Free PMC Article
    2. PRIMA-1MET inhibits growth of mouse tumors carrying mutant p53. Zache N, et al. Cell Oncol, 2008. PMID 18791272, Free PMC Article
    3. Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes. Noureddine H, et al. J Biol Chem, 2007 Feb 9. PMID 17158452
    4. The AChE membrane-binding tail PRiMA is down-regulated in muscle and nerve of mice with muscular dystrophy by merosin deficiency. Vidal CJ, et al. Chem Biol Interact, 2013 Mar 25. PMID 22906800
    5. Developmental adaptation of central nervous system to extremely high acetylcholine levels. Farar V, et al. PLoS One, 2013. PMID 23861875, Free PMC Article

    See all (31) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. It interacts with PS1 and undergoes proteolytic processing.
      Title: Presenilin-1 influences processing of the acetylcholinesterase membrane anchor PRiMA.
    2. Elevated expression of muscarinic receptors is responsible for physiological adaptation of PRiMA-deficient developing mice.
      Title: Developmental adaptation of central nervous system to extremely high acetylcholine levels.
    3. the relative content of AChE, BuChE and PRiMA mRNAs were compared in normal and Lama2dy muscle and sciatic nerve
      Title: The AChE membrane-binding tail PRiMA is down-regulated in muscle and nerve of mice with muscular dystrophy by merosin deficiency.
    4. The N-linked glycosylation of AChE(T) plays a major role for acquisition of AChE full enzymatic activity but does not affect its oligomerization.
      Title: The assembly of proline-rich membrane anchor (PRiMA)-linked acetylcholinesterase enzyme: glycosylation is required for enzymatic activity but not for oligomerization.
    5. Data show that along the nerve terminus the vast majority of acetylcholinesterase is anchored by collagen Q that is only produced by the muscle, whereas very minor amounts of AChE are anchored by PRiMA that is produced by motoneurons.
      Title: Distinct localization of collagen Q and PRiMA forms of acetylcholinesterase at the neuromuscular junction.
    6. Proline-rich membrane anchor protein is necessary to target and/or to stabilize nascent acetylcholinesterase in neurons.
      Title: Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit.
    7. PRIMA-1MET targets mouse tumors carrying mutant p53
      Title: PRIMA-1MET inhibits growth of mouse tumors carrying mutant p53.
    8. Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA
      Title: Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA.
    9. PRiMA expression is predominantly to the cholinergic system and that anchoring of cholinesterases to cell membranes by PRiMA represents a limiting factor for production of the AChE tailed splice variant (AChET)-PRiMA complex.
      Title: Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase.
    10. expression of PRiMA, as well as PRiMA-associated G(4) AChE, in muscle is suppressed by muscle regulatory factors, muscular activity, and nerve-derived trophic factors
      Title: Regulation of a transcript encoding the proline-rich membrane anchor of globular muscle acetylcholinesterase. The suppressive roles of myogenesis and innervating nerves.
    Submit: New GeneRIF Correction See all GeneRIFs (11)

    Variation

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    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)
    • Endonuclease-mediated (3) 
    • Targeted (1)  1 citation

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    enables enzyme binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein-membrane adaptor activity IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within establishment of localization in cell IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in anchoring junction IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in synapse IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    proline-rich membrane anchor 1
    Names
    acetylcholinesterase membrane anchor

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_133364.2 → NP_579942.2  proline-rich membrane anchor 1 precursor

      Status: VALIDATED

      Source sequence(s)
      AK039705, AK140034, AY043275
      Consensus CDS
      CCDS26127.1
      UniProtKB/Swiss-Prot
      Q810F0, Q8VHC4
      UniProtKB/TrEMBL
      F8VQJ2
      Related
      ENSMUSP00000074017.4, ENSMUST00000074416.10
      Conserved Domains (1) summary
      pfam16101
      Location:37 → 153
      PRIMA1; Proline-rich membrane anchor 1

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000078.7 Reference GRCm39 C57BL/6J

      Range
      103160712..103208967 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006515507.5 → XP_006515570.1  proline-rich membrane anchor 1 isoform X1

      UniProtKB/Swiss-Prot
      Q810F0, Q8VHC4
      UniProtKB/TrEMBL
      F8VQJ2
      Conserved Domains (1) summary
      pfam16101
      Location:37 → 153
      PRIMA1; Proline-rich membrane anchor 1

    2. XM_006515506.3 → XP_006515569.1  proline-rich membrane anchor 1 isoform X1

      UniProtKB/Swiss-Prot
      Q810F0, Q8VHC4
      UniProtKB/TrEMBL
      F8VQJ2
      Conserved Domains (1) summary
      pfam16101
      Location:37 → 153
      PRIMA1; Proline-rich membrane anchor 1

    RNA

    1. XR_381482.2 RNA Sequence

    2. XR_381481.2 RNA Sequence

      Related
      ENSMUST00000127843.8

    Suppressed Reference Sequence(s)

    The following Reference Sequences have been suppressed. Explain

    1. NM_178023.2: Suppressed sequence

      Description
      NM_178023.2: This RefSeq was permanently suppressed because it is a nonsense-mediated mRNA decay (NMD) candidate.
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q810F0.2 GenPept UniProtKB/Swiss-Prot:Q810F0

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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